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Protein

Glutathione S-transferase class-mu 26 kDa isozyme

Gene
N/A
Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111SubstrateCurated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 5607.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 26 kDa isozyme (EC:2.5.1.18)
Short name:
GST 26
Alternative name(s):
Sj26 antigen
SjGST
OrganismiSchistosoma japonicum (Blood fluke)
Taxonomic identifieri6182 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001858052 – 218Glutathione S-transferase class-mu 26 kDa isozymeAdd BLAST217

Proteomic databases

PRIDEiP08515.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi9 – 11Combined sources3
Helixi12 – 14Combined sources3
Helixi15 – 21Combined sources7
Beta strandi29 – 31Combined sources3
Helixi35 – 37Combined sources3
Helixi38 – 42Combined sources5
Turni43 – 46Combined sources4
Beta strandi55 – 59Combined sources5
Beta strandi64 – 67Combined sources4
Helixi68 – 72Combined sources5
Helixi77 – 79Combined sources3
Helixi86 – 107Combined sources22
Turni108 – 111Combined sources4
Helixi115 – 136Combined sources22
Turni137 – 139Combined sources3
Beta strandi145 – 147Combined sources3
Helixi150 – 162Combined sources13
Turni163 – 165Combined sources3
Turni167 – 172Combined sources6
Helixi174 – 184Combined sources11
Helixi187 – 193Combined sources7
Beta strandi195 – 197Combined sources3
Beta strandi203 – 207Combined sources5
Beta strandi209 – 211Combined sources3
Beta strandi213 – 215Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8XX-ray2.70A2-218[»]
1BG5X-ray2.60A1-218[»]
1DUGX-ray1.80A/B2-218[»]
1GNEX-ray2.50A2-218[»]
1GTAX-ray2.40A1-218[»]
1GTBX-ray2.60A1-218[»]
1M99X-ray2.30A1-218[»]
1M9AX-ray2.10A1-218[»]
1M9BX-ray2.60A1-218[»]
1U87X-ray3.50A1-218[»]
1U88X-ray3.50A/B1-218[»]
1UA5X-ray2.50A1-218[»]
1Y6EX-ray3.00A/B2-218[»]
3CRTX-ray1.90A1-214[»]
3CRUX-ray2.30A1-214[»]
3D0ZX-ray2.50A1-214[»]
3QMZX-ray6.00S/T2-218[»]
4AI6X-ray3.40A/B2-218[»]
4AKGX-ray3.30A/B2-218[»]
4AKHX-ray3.60A/B2-218[»]
4AKIX-ray3.70A/B2-218[»]
4ECBX-ray2.20A/B1-218[»]
4ECCX-ray2.20A1-215[»]
4WR4X-ray1.60A2-218[»]
4WR5X-ray1.93A2-218[»]
ProteinModelPortaliP08515.
SMRiP08515.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 83GST N-terminalAdd BLAST82
Domaini85 – 203GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione binding1 Publication1 Publication2
Regioni41 – 45Glutathione binding1 Publication1 Publication5
Regioni54 – 55Glutathione binding1 Publication1 Publication2
Regioni67 – 68Glutathione binding1 Publication1 Publication2

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL
60 70 80 90 100
EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL
110 120 130 140 150
DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH
160 170 180 190 200
PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA
210
WPLQGWQATF GGGDHPPK
Length:218
Mass (Da):25,499
Last modified:January 23, 2007 - v3
Checksum:i5E2AC418BD0EF13F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14654 mRNA. Translation: AAB59203.1.
PIRiA61514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14654 mRNA. Translation: AAB59203.1.
PIRiA61514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8XX-ray2.70A2-218[»]
1BG5X-ray2.60A1-218[»]
1DUGX-ray1.80A/B2-218[»]
1GNEX-ray2.50A2-218[»]
1GTAX-ray2.40A1-218[»]
1GTBX-ray2.60A1-218[»]
1M99X-ray2.30A1-218[»]
1M9AX-ray2.10A1-218[»]
1M9BX-ray2.60A1-218[»]
1U87X-ray3.50A1-218[»]
1U88X-ray3.50A/B1-218[»]
1UA5X-ray2.50A1-218[»]
1Y6EX-ray3.00A/B2-218[»]
3CRTX-ray1.90A1-214[»]
3CRUX-ray2.30A1-214[»]
3D0ZX-ray2.50A1-214[»]
3QMZX-ray6.00S/T2-218[»]
4AI6X-ray3.40A/B2-218[»]
4AKGX-ray3.30A/B2-218[»]
4AKHX-ray3.60A/B2-218[»]
4AKIX-ray3.70A/B2-218[»]
4ECBX-ray2.20A/B1-218[»]
4ECCX-ray2.20A1-215[»]
4WR4X-ray1.60A2-218[»]
4WR5X-ray1.93A2-218[»]
ProteinModelPortaliP08515.
SMRiP08515.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP08515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.5.1.18. 5607.

Miscellaneous databases

EvolutionaryTraceiP08515.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGST26_SCHJA
AccessioniPrimary (citable) accession number: P08515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

There are at least two isoenzymes of GST in S.japonicum.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.